2hlc
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hlc OCA], [http://www.ebi.ac.uk/pdbsum/2hlc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hlc RCSB]</span> | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:31:59 2008'' |
Revision as of 00:32, 31 March 2008
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| , resolution 1.7Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HL COLLAGENASE STRUCTURE AT 1.7A RESOLUTION
Overview
Collagenase from the fly larvae Hypoderma lineatum cleaves triple-helical collagen in a single region. It was crystallized at neutral pH in the absence of inhibitor and 1.8 A data were collected using synchrotron radiation and a Mark II prototype detector. The structure was solved by combining multiple isomorphous replacement methods and rotation translation function in real space. Refinement between 7 and 1.8 A using the program X-PLOR led to a final R factor of 16.9%. The overall fold is similar to that of other trypsin-like enzymes but the structure differs mainly by the presence of a beta-sheet at position 31-44. The two embedded molecules of the asymmetric unit are related by a pseudo twofold axis. The beta-sheet 31-44 of one molecule is involved in hydrogen bonds with binding-pocket residues of the other molecule. It thus completely prevents access to the active site. The specificity of this enzyme probably results from the position of Phe192 and Tyr99 at the entrance of the active site.
About this Structure
2HLC is a Single protein structure of sequence from Hypoderma lineatum. Full crystallographic information is available from OCA.
Reference
1.8 A structure of Hypoderma lineatum collagenase: a member of the serine proteinase family., Broutin I, Arnoux B, Riche C, Lecroisey A, Keil B, Pascard C, Ducruix A, Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):380-92. PMID:15299709
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